The structure of chromophore-grafted Amyloid-β 12-28 dimers in the gas-phase: FRET-experiments guided modelling - Archive ouverte HAL Access content directly
Journal Articles Physical Chemistry Chemical Physics Year : 2016

The structure of chromophore-grafted Amyloid-β 12-28 dimers in the gas-phase: FRET-experiments guided modelling

Abstract

We present theoretical modelling, ion mobility spectrometry and action-FRET experiments for chromophore-grafted amyloid-β12–28 dimers. A first-principles global minimum search based on replica-exchange molecular dynamics (REMD) leads to a compact structure with strong interstrand interactions. We use REMD with a distance restraint that implements an adaptive effective bias upon average FRET-efficiencies and thus guides the sampling by the action-FRET measurement. This procedure leads to a pair of weakly interacting peptides. Ion-mobility confirms that the weakly interacting structure and not the global minimum with strongly interacting peptides is populated in the experiment. The presence of a high energy barrier between the two structural families, as evidenced from the MD data, suggests that a kinetically trapped structure is observed in the experiment.
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Dates and versions

hal-01344513 , version 1 (12-07-2016)

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Alexander Kulesza, Steven Daly, Chang Min Choi, Anne-Laure Simon, Fabien Chirot, et al.. The structure of chromophore-grafted Amyloid-β 12-28 dimers in the gas-phase: FRET-experiments guided modelling. Physical Chemistry Chemical Physics, 2016, 18 (13), pp.9061-9069. ⟨10.1039/c6cp00263c⟩. ⟨hal-01344513⟩
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